dbPTM

LAT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LAT_HUMAN
UniProt AC	O43561
Protein Name	Linker for activation of T-cells family member 1
Gene Name	LAT
Organism	Homo sapiens (Human).
Sequence Length	262
Subcellular Localization	Cell membrane Single-pass type III membrane protein . Present in lipid rafts.
Protein Description	Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules..
Protein Sequence	MEEAILVPCVLGLLLLPILAMLMALCVHCHRLPGSYDSTSSDSLYPRGIQFKRPHTVAPWPPAYPPVTSYPPLSQPDLLPIPRSPQPLGGSHRTPSSRRDSDGANSVASYENEGASGIRGAQAGWGVWGPSWTRLTPVSLPPEPACEDADEDEDDYHNPGYLVVLPDSTPATSTAAPSAPALSTPGIRDSAFSMESIDDYVNVPESGESAEASLDGSREYVNVSQELHPGAAKTEPAALSSQEAEEVEEEGAPDYENLQELN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
26	S-palmitoylation	LAMLMALCVHCHRLP HHHHHHHHHHHHCCC	1.11	9729044
29	S-palmitoylation	LMALCVHCHRLPGSY HHHHHHHHHCCCCCC	0.71	9729044
29 (in isoform 3)	Phosphorylation	-	0.71	24719451
29	Phosphorylation	LMALCVHCHRLPGSY HHHHHHHHHCCCCCC	0.71	24719451
35	Phosphorylation	HCHRLPGSYDSTSSD HHHCCCCCCCCCCCC	24.67	21082442
36	Phosphorylation	CHRLPGSYDSTSSDS HHCCCCCCCCCCCCC	21.59	28796482
38	Phosphorylation	RLPGSYDSTSSDSLY CCCCCCCCCCCCCCC	23.19	25072903
38	O-linked_Glycosylation	RLPGSYDSTSSDSLY CCCCCCCCCCCCCCC	23.19	OGP
39	Phosphorylation	LPGSYDSTSSDSLYP CCCCCCCCCCCCCCC	29.38	21082442
39	O-linked_Glycosylation	LPGSYDSTSSDSLYP CCCCCCCCCCCCCCC	29.38	OGP
40	Phosphorylation	PGSYDSTSSDSLYPR CCCCCCCCCCCCCCC	35.78	23401153
41	Phosphorylation	GSYDSTSSDSLYPRG CCCCCCCCCCCCCCC	31.16	21082442
43	Phosphorylation	YDSTSSDSLYPRGIQ CCCCCCCCCCCCCCC	31.58	21082442
45	Phosphorylation	STSSDSLYPRGIQFK CCCCCCCCCCCCCCC	8.54	19605366
52	Ubiquitination	YPRGIQFKRPHTVAP CCCCCCCCCCCCCCC	48.95	-
64	Phosphorylation	VAPWPPAYPPVTSYP CCCCCCCCCCCCCCC	17.53	27642862
68	Phosphorylation	PPAYPPVTSYPPLSQ CCCCCCCCCCCCCCC	28.46	28270605
68	O-linked_Glycosylation	PPAYPPVTSYPPLSQ CCCCCCCCCCCCCCC	28.46	OGP
69	Phosphorylation	PAYPPVTSYPPLSQP CCCCCCCCCCCCCCC	35.56	27642862
70	Phosphorylation	AYPPVTSYPPLSQPD CCCCCCCCCCCCCCC	10.25	28270605
74	Phosphorylation	VTSYPPLSQPDLLPI CCCCCCCCCCCCCCC	45.50	28270605
74	O-linked_Glycosylation	VTSYPPLSQPDLLPI CCCCCCCCCCCCCCC	45.50	OGP
75	Phosphorylation	TSYPPLSQPDLLPIP CCCCCCCCCCCCCCC	43.12	27251275
83 (in isoform 4)	Phosphorylation	-	62.78	15659558
83 (in isoform 5)	Phosphorylation	-	62.78	15659558
84	O-linked_Glycosylation	DLLPIPRSPQPLGGS CCCCCCCCCCCCCCC	23.64	OGP
84	Phosphorylation	DLLPIPRSPQPLGGS CCCCCCCCCCCCCCC	23.64	23401153
88	Ubiquitination	IPRSPQPLGGSHRTP CCCCCCCCCCCCCCC	11.62	-
90 (in isoform 5)	Phosphorylation	-	28.14	28634298
90 (in isoform 4)	Phosphorylation	-	28.14	28634298
91	Phosphorylation	SPQPLGGSHRTPSSR CCCCCCCCCCCCCCC	14.16	24702127
94	Phosphorylation	PLGGSHRTPSSRRDS CCCCCCCCCCCCCCC	23.30	26074081
96	Phosphorylation	GGSHRTPSSRRDSDG CCCCCCCCCCCCCCC	35.54	26074081
97	Phosphorylation	GSHRTPSSRRDSDGA CCCCCCCCCCCCCCC	32.32	26074081
101	Phosphorylation	TPSSRRDSDGANSVA CCCCCCCCCCCCCCH	35.81	23401153
106	Phosphorylation	RDSDGANSVASYENE CCCCCCCCCHHHHCC	20.66	28787133
109 (in isoform 4)	Phosphorylation	-	30.72	-
109	Phosphorylation	DGANSVASYENEGAS CCCCCCHHHHCCCCC	30.72	19690332
110	Phosphorylation	GANSVASYENEGASG CCCCCHHHHCCCCCC	17.03	28796482
110 (in isoform 2)	Phosphorylation	-	17.03	-
116	Phosphorylation	SYENEGASGIRGAQA HHHCCCCCCCCCCCC	45.68	28450419
120	Phosphorylation	EGASGIRGAQAGWGV CCCCCCCCCCCCCCC	21.81	27251275
131	Phosphorylation	GWGVWGPSWTRLTPV CCCCCCCCCCCCCCC	36.82	24850871
133	Phosphorylation	GVWGPSWTRLTPVSL CCCCCCCCCCCCCCC	21.82	28122231
146 (in isoform 3)	Phosphorylation	-	7.71	-
156	Phosphorylation	ADEDEDDYHNPGYLV CCCCCCCCCCCCEEE	18.80	11368773
161	Phosphorylation	DDYHNPGYLVVLPDS CCCCCCCEEEEECCC	9.51	16081816
173	O-linked_Glycosylation	PDSTPATSTAAPSAP CCCCCCCCCCCCCCC	20.39	29351928
174	O-linked_Glycosylation	DSTPATSTAAPSAPA CCCCCCCCCCCCCCC	23.60	OGP
178	O-linked_Glycosylation	ATSTAAPSAPALSTP CCCCCCCCCCCCCCC	42.00	29351928
178	Phosphorylation	ATSTAAPSAPALSTP CCCCCCCCCCCCCCC	42.00	26074081
183	Phosphorylation	APSAPALSTPGIRDS CCCCCCCCCCCCCCC	34.36	26074081
184	Phosphorylation	PSAPALSTPGIRDSA CCCCCCCCCCCCCCC	26.78	26074081
190	Phosphorylation	STPGIRDSAFSMESI CCCCCCCCCCCCCCC	22.74	26074081
193	Phosphorylation	GIRDSAFSMESIDDY CCCCCCCCCCCCHHH	22.74	28634120
196	Phosphorylation	DSAFSMESIDDYVNV CCCCCCCCCHHHCCC	23.75	28634120
200	Phosphorylation	SMESIDDYVNVPESG CCCCCHHHCCCCCCC	7.09	29978859
206	Phosphorylation	DYVNVPESGESAEAS HHCCCCCCCCCCCCC	41.62	29978859
209	Phosphorylation	NVPESGESAEASLDG CCCCCCCCCCCCCCC	34.63	28634120
213	Phosphorylation	SGESAEASLDGSREY CCCCCCCCCCCCCCE	20.64	28270605
217	Phosphorylation	AEASLDGSREYVNVS CCCCCCCCCCEEECC	22.93	28270605
220	Phosphorylation	SLDGSREYVNVSQEL CCCCCCCEEECCCCC	9.01	15570572
224	Phosphorylation	SREYVNVSQELHPGA CCCEEECCCCCCCCC	16.85	23401153
231	Phosphorylation	SQELHPGAAKTEPAA CCCCCCCCCCCCCCC	15.38	27251275
234	Phosphorylation	LHPGAAKTEPAALSS CCCCCCCCCCCCCCH	42.34	28270605
240	Phosphorylation	KTEPAALSSQEAEEV CCCCCCCCHHHHHHH	25.83	30576142
241	Phosphorylation	TEPAALSSQEAEEVE CCCCCCCHHHHHHHH	32.65	30576142
255	Phosphorylation	EEEGAPDYENLQELN HHCCCCCHHHHHHCC	12.98	19605366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
127	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
132	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
155	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
155	T	Phosphorylation	Kinase	MAPK8	P45983	GPS
171	Y	Phosphorylation	Kinase	PTK2	Q05397	GPS
171	Y	Phosphorylation	Kinase	PTK2B	Q14289	GPS
171	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
191	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
226	Y	Phosphorylation	Kinase	ZAP70	P43403	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:23514740

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
26	C	Palmitoylation	9729044
Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation.
26	C	Phosphorylation	9729044
Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation.
29	C	Palmitoylation	9729044
Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation.
29	C	Phosphorylation	9729044
Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of LAT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITK_HUMAN	ITK	physical	10506192
GRB2_HUMAN	GRB2	physical	11368773
PLCG1_HUMAN	PLCG1	physical	11368773
P85A_HUMAN	PIK3R1	physical	11368773
CLYBL_HUMAN	CLYBL	physical	11368773
VAV_HUMAN	VAV1	physical	11368773
GRB2_HUMAN	GRB2	physical	9489702
GRAP_HUMAN	GRAP	physical	9489702
PLCG1_HUMAN	PLCG1	physical	9489702
GRAP2_HUMAN	GRAP2	physical	10021361
GRAP_HUMAN	GRAP	physical	12186560
GRB2_HUMAN	GRB2	physical	12186560
VAV_HUMAN	VAV1	physical	12186560
M4K1_HUMAN	MAP4K1	physical	11279207
CD3Z_HUMAN	CD247	physical	14523017
LCK_HUMAN	LCK	physical	14523017
CD3E_HUMAN	CD3E	physical	14523017
LCK_HUMAN	LCK	physical	16938345
PLCG1_HUMAN	PLCG1	physical	16938345
CBL_HUMAN	CBL	physical	16938345
SPY1_HUMAN	SPRY1	physical	19915061
ZAP70_HUMAN	ZAP70	physical	16906159
PLCG1_HUMAN	PLCG1	physical	16467851
ZAP70_HUMAN	ZAP70	physical	23514740
LCP2_HUMAN	LCP2	physical	23514740
ZHX2_HUMAN	ZHX2	physical	21988832
TRAF6_HUMAN	TRAF6	physical	25907557
US03_HHV11	US3	physical	25907557
GG_HHV11	US3	physical	25907557
PLCG1_HUMAN	PLCG1	physical	27221712
PLCG2_HUMAN	PLCG2	physical	27221712
PTN6_HUMAN	PTPN6	physical	27221712

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LAT_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"LAT palmitoylation: its essential role in membrane microdomaintargeting and tyrosine phosphorylation during T cell activation."; Zhang W., Trible R.P., Samelson L.E.; Immunity 9:239-246(1998). Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-26 AND CYS-29, ANDMUTAGENESIS OF CYS-26 AND CYS-29.	9729044 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; THR-39; SER-40;SER-41; SER-43; SER-101; SER-106; SER-240; SER-241 AND TYR-255, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39; SER-84; SER-101;SER-109 AND SER-224, AND MASS SPECTROMETRY.	18088087 [Abstract]
"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptorto cellular activation."; Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; Cell 92:83-92(1998). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCEOF 32-47 AND 219-233, PHOSPHORYLATION AT TYR-200, MASS SPECTROMETRY,MUTAGENESIS OF TYR-200 AND TYR-220, TISSUE SPECIFICITY, SUBCELLULARLOCATION, AND INTERACTION WITH PIK3R1; GRB2; GRAP AND PLCG1.	9489702 [Abstract]

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